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UniProtKB/Swiss-Prot entry Q15311


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RBP1_HUMAN
Primary accession number Q15311
Secondary accession numbers None
Integrated into Swiss-Prot on August 15, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 75)
Name and origin of the protein
Protein name RalA-binding protein 1
Synonyms RalBP1
Ral-interacting protein 1
76 kDa Ral-interacting protein
Dinitrophenyl S-glutathione ATPase
DNP-SG ATPase
Gene name
Name: RALBP1
Synonyms: RLIP1, RLIP76
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RALA.
DOI=10.1074/jbc.270.38.22473; PubMed=7673236 [NCBI, ExPASy, EBI, Israel, Japan]
Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.;
"Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity.";
J. Biol. Chem. 270:22473-22477(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND PROTEIN SEQUENCE OF 2-15; 409-438 AND 472-486.
TISSUE=Bone marrow;
DOI=10.1021/bi992964c; PubMed=10924126 [NCBI, ExPASy, EBI, Israel, Japan]
Awasthi S., Cheng J., Singhal S.S., Saini M.K., Pandya U., Pikula S., Bandorowicz-Pikula J., Singh S.V., Zimniak P., Awasthi Y.C.;
"Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin.";
Biochemistry 39:9327-9334(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH REPS2.
TISSUE=Brain;
DOI=10.1074/jbc.273.2.814; PubMed=9422736 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.;
"Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral.";
J. Biol. Chem. 273:814-821(1998).
[5]
FUNCTION, AND INTERACTION WITH CCNB1; CDC2; EPN1; NUMB AND TFAP2A.
DOI=10.1074/jbc.M302191200; PubMed=12775724 [NCBI, ExPASy, EBI, Israel, Japan]
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1006/abbi.2001.2395; PubMed=11437348 [NCBI, ExPASy, EBI, Israel, Japan]
Sharma R., Singhal S.S., Cheng J., Yang Y., Sharma A., Zimniak P., Awasthi S., Awasthi Y.C.;
"RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes.";
Arch. Biochem. Biophys. 391:171-179(2001).
[7]
INTERACTION WITH DAB2IP.
DOI=10.1074/jbc.M407617200; PubMed=15310755 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.;
"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation.";
J. Biol. Chem. 279:44955-44965(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-29, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-62, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin.
  • SUBUNIT: Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDC2 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis.
  • SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
  • TISSUE SPECIFICITY: Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.
  • SIMILARITY: Contains 1 Rho-GAP domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L42542; AAB00103.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013126; AAH13126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00009544; -.
PIR F59435; F59435.
RefSeq NP_006779.1; -.
UniGene Hs.528993
3D structure databases
ModBase Q15311.
Protein-protein interaction databases
IntAct Q15311; 3.
Protein family/group databases
TCDB 9.A.1.1.1; non ABC multidrug exporter (N-MDE) family.
PTM databases
PhosphoSite Q15311; -.
Enzyme and pathway databases
Reactome REACT_11044; Signaling by Rho GTPases.
Organism-specific databases
GeneCards GC18P009465; -.
H-InvDB HIX0014325; -.
HGNC HGNC:9841; RALBP1.
GenAtlas RALBP1.
MIM 605801; gene. [NCBI / EBI]
PharmGKB PA34199; -.
Gene expression databases
ArrayExpress Q15311; -.
Bgee Q15311; -.
CleanEx HS_RALBP1; -.
GermOnline ENSG00000017797; Homo sapiens.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0016020; Cellular component: membrane (inferred from direct assay from UniProtKB).
GO:0043492; Molecular function: ATPase activity, coupled to movement of substances (inferred from direct assay from UniProtKB).
GO:0030675; Molecular function: Rac GTPase activator activity (inferred from direct assay from UniProtKB).
GO:0048365; Molecular function: Rac GTPase binding (inferred from physical interaction from UniProtKB).
GO:0017160; Molecular function: Ral GTPase binding (inferred from physical interaction from UniProtKB).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0043089; Biological process: positive regulation of Cdc42 GTPase activity (inferred from direct assay from UniProtKB).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from physical interaction from UniProtKB).
GO:0006810; Biological process: transport (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000198; RhoGAP.
Graphical view of domain structure.
Gene3D G3DSA:1.10.555.10; RhoGAP; 1.
Pfam PF00620; RhoGAP; 1.
Pfam graphical view of domain structure.
SMART SM00324; RhoGAP; 1.
SMART graphical view of domain structure.
PROSITE PS50238; RHOGAP; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q15311; -.
PRIDE Q15311; -.
Genome annotation databases
Ensembl ENSG00000017797; Homo sapiens. [Contig view]
GeneID 10928; -.
KEGG hsa:10928; -.
Phylogenomic databases
HOGENOM Q15311; -.
HOVERGEN Q15311; -.
OMA Q15311; TQAGIKE.
Other
NextBio 41515; -.
SOURCE RALBP1; Homo sapiens.
ProtoNet Q15311.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; GTPase activation; Membrane; Phosphoprotein; Polymorphism; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   655  654     RalA-binding protein 1. PRO_0000056733
DOMAIN   192   380  189     Rho-GAP. 
REGION   403   499  97     Interacts with RalA. 
COMPBIAS   164   171  8     Poly-Lys. 
MOD_RES   27    27        Phosphothreonine. 
MOD_RES   29    29        Phosphoserine. 
MOD_RES   34    34        Phosphoserine. 
MOD_RES   62    62        Phosphoserine. 
MOD_RES   92    92        Phosphoserine. 
MOD_RES   93    93        Phosphoserine. 
VARIANT   617   617  1     A -> V (in dbSNP:rs35867116 [NCBI]). VAR_049147 
Sequence information
Length: 655 AA [This is the length of the unprocessed precursor] Molecular weight: 76063 Da [This is the MW of the unprocessed precursor] CRC64: EC6F75329FD8D062 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDILHEPPDV 

        70         80         90        100        110        120 
VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKMKRSKGIH VFKKPSFSKK 

       130        140        150        160        170        180 
KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ 

       190        200        210        220        230        240 
IDVPNLKPIF GIPLADAVER TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV 

       250        260        270        280        290        300 
DELKAAYDRE ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV 

       310        320        330        340        350        360 
QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVF 

       370        380        390        400        410        420 
FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI 

       430        440        450        460        470        480 
KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN 

       490        500        510        520        530        540 
ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS 

       550        560        570        580        590        600 
ESESESEDEE ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK 

       610        620        630        640        650 
AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR KETSI 

Q15311 in FASTA format

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